title: FACT and the reorganized nucleosome.
abstract: FACT is an essential component of the machinery used by eukaryotic cells both to establish and to overcome the nucleosomal barrier to DNA accessibility, and it does so without hydrolyzing ATP. FACT is a transcription elongation factor, but this review stresses additional roles in DNA replication and initiation of transcription. The widely-held model that FACT functions by displacing an H2A-H2B dimer from a nucleosome is examined, and an alternative proposal is presented in which dimer loss can occur but is a secondary effect of a primary structural change induced by FACT binding which we have called "nucleosome reorganization." The structures of two domains of FACT have been determined and they reveal multiple potential interaction sites. Roles for these binding sites in FACT function and regulation are discussed.
authors.affiliation: University of Utah School of Medicine, Department of Biochemistry, 15 N Medical Drive East RM 4100, Salt Lake City, UT 84112-5650, USA. Tim@biochem.utah.edu
authors.forename: Tim
authors.initials: T
authors.lastname: Formosa
mesh_terms: D000818:Animals; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism; D004261:DNA Replication; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism; D006655:Histone Deacetylases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D009707:Nucleosomes / Q000378:metabolism*; D010641:Phenotype; D014158:Transcription, Genetic; D035602:Transcriptional Elongation Factors / Q000737:chemistry* / Q000378:metabolism
chemical_list: D002843:Chromatin; D009707:Nucleosomes; D035602:Transcriptional Elongation Factors; D051548:Histone Acetyltransferases; D006655:Histone Deacetylases